| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB32051-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF3205-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1384SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-58358SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-22117SS | |||
| Azide and BSA Free | NBP2-81014 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | MAB8094-SP | |||
![Western Blot: Yes Antibody (2D5) [H00007525-M03] - Analysis of YES1 expression in A-431 (Cat # L015V1).](http://images.novusbio.com/fullsize/Yes-Antibody-2D5-Western-Blot-H00007525-M03-img0005.jpg "Western Blot: Yes Antibody (2D5) [H00007525-M03] - Analysis of YES1 expression in A-431 (Cat # L015V1).")
![Immunohistochemistry-Paraffin: Yes Antibody (2D5) [H00007525-M03] - Analysis of monoclonal antibody to YES1 on formalin-fixed paraffin-embedded human smooth muscle. Antibody concentration 3 ug/ml](http://images.novusbio.com/fullsize/Yes-Antibody-2D5-Immunohistochemistry-Paraffin-H00007525-M03-img0003.jpg)
![Sandwich ELISA: Yes Antibody (2D5) [H00007525-M03] - Detection limit for recombinant GST tagged YES1 is approximately 10ng/ml as a capture antibody.](http://images.novusbio.com/fullsize/Yes-Antibody-2D5-Sandwich-ELISA-H00007525-M03-img0004.jpg)
![Western Blot: Yes Antibody (2F4) [H00007525-M01] - Analysis of YES1 over-expressed 293 cell line, cotransfected with YES1 Validated Chimera RNAi ( Cat # H00007525-R01V ) (Lane 2) or non-transfected control (Lane 1). Blot probed with YES1 monoclonal antibody (M01) clone 2F4 (Cat # H00007525-M01 ). GAPDH ( 36.1 kDa ) used as specificity and loading control.](http://images.novusbio.com/fullsize/Yes-Antibody-2F4-Western-Blot-H00007525-M01-img0003.jpg "Western Blot: Yes Antibody (2F4) [H00007525-M01] - Analysis of YES1 over-expressed 293 cell line, cotransfected with YES1 Validated Chimera RNAi ( Cat # H00007525-R01V ) (Lane 2) or non-transfected control (Lane 1). Blot probed with YES1 monoclonal antibody (M01) clone 2F4 (Cat # H00007525-M01 ). GAPDH ( 36.1 kDa ) used as specificity and loading control.")
![Western Blot: Yes Antibody (2F4) [H00007525-M01] - Analysis of YES1 expression in transfected 293T cell line by YES1 monoclonal antibody (M01), clone 2F4.Lane 1: YES1 transfected lysate(59.84 KDa).Lane 2: Non-transfected lysate.](http://images.novusbio.com/fullsize/Yes-Antibody-2F4-Western-Blot-H00007525-M01-img0004.jpg)
![Western Blot: Yes Antibody (S07-8B3) [NBP3-19980] - Western blot detection of Yes in K562 cell lysates using NBP3-19980 (1:1000 diluted). Predicted band size: 61kDa. Observed band size: 61kDa.](http://images.novusbio.com/fullsize/Yes-Antibody-S07-8B3-Western-Blot-NBP3-19980-img0001.jpg "Western Blot: Yes Antibody (S07-8B3) [NBP3-19980] - Western blot detection of Yes in K562 cell lysates using NBP3-19980 (1:1000 diluted). Predicted band size: 61kDa. Observed band size: 61kDa.")
![Analysis of LC3B in HeLa cells using anti-LC3B antibody (red) [Catalog # NB600-1384]. Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB600-1384-img0033.jpg)
![Analysis of LC3B in treated U87-MG (human glioblastoma astrocytoma) lysates using anti- [Catalog # NB600-1384].](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Western-Blot-NB600-1384-img0027.jpg)
![Staining of treated U373-MG (human glioblastoma) cells using anti- [Catalog # NB600-1384].](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB600-1384-img0030.jpg)
![Analysis of U87MG glioma xenografts using anti- [Catalog # NB600-1384]. Image from verified customer review.](http://images.novusbio.com/fullsize/LC3B-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB600-1384-img0023.jpg)
![Immunocytochemistry/ Immunofluorescence: LC3B Antibody - BSA Free [NB600-1384] - Assesment of functional basal autophagy in vitro(A) Immunoblotting of LC3B & p62 upon pharmacological autophagy inhibition. A dose-dependent increase of LC3B & p62 was observed with increasing concentrations of chloroquine. (B) Immunofluorescence of LC3B & p62 upon pharmacological autophagy inhibition. I. In CC cell lines HT-29 & II. LoVo a dose-dependent increase of LC3B & p62 was observed with increasing concentrations of chloroquine. (C) Electron microscopy of CC cell lines pharmacological autophagy inhibition. I-III. In CC cell line HT-29 a dose-dependent increase of cytoplasmic vesicles was observed with increasing concentrations of CQ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28903368), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202415384116.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Phosphorylation of AKT & mTOR decreases after treatment with gemcitabine (GCB)A LM7, CCH-OS-D, & K7M3 osteosarcoma cells were treated with 1μM GCB & cell lysates were analyzed by immunoblotting with specific antibodies for AKT, mTOR, p-AKT, & p-mTOR. beta -actin was used as a loading control. Densitometry was performed using ImageJ. B. & C. Following treatment with GCB, lysates were analyzed using the Human Phospho Kinase Antibody Array. The phosphorylation levels of AKT, mTOR, PRAS40, p70S6K, JNK, AMPK, & ERK were evaluated. Densitometry was performed using Image J. Values were graphed as relative fold change. Means ± standard deviation of three independent experiments are shown. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.20308), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202415304227.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Autophagy decreases during striatal development. (A) Representative Western blot images for LC3B, p62, DARPP32, & actin. Quantification of (B) LC3B-ii relative to actin, (C) LC3B-ii relative to LC3B-i, (D) p62 relative to actin normalized to P120 values. Data analyzed with one-way ANOVA; (B) Age: F(4,21) = 6.526, p = 0.0014; (C) Age: F(4,22) = 3.797, p = 0.0171; (D) Age: F(4,15) = 3.762, p = 0.0260. *p 0.01); (b) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. Flow cytometry was performed for measuring the ROS level by a DCFH-DA probe in indicated cells. Rap, rapamycin. (n = 3, *P 0.01); (c) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & then starved by HBSS for 3 h. ATP levels were detected by ATP Assay Kit (n = 3, *P > 0.01); (d) FTC-133/TPC-1 cells were pretreated with NAC (2 mM) & then starved by HBSS for 3 h. LC3-I/II, NIS, p-AMPK, AMPK, p-mTOR, mTOR, p-p70S6K & p70S6K levels were assayed by Western blot; (e) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. LC3-I/II, NIS, p-mTOR & mTOR levels were assayed by Western blot. Rap, rapamycin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241617143.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Serum starvation induces autophagy & apoptosis in endothelial cells.A Evaluation by Hoechst 33342 & propidium iodide (HO/PI) staining of apoptosis & necrosis in HUVECs exposed to normal medium (N) or serum-starved (SS) for 4 h. P values obtained by unpaired t test. n = 10 for each condition. Scale bar = 25 μm. B Quantification of caspase-3 activity in HUVECs exposed to N or SS HUVECs for 1, 2, 3, & 4 h. P values obtained by one-way ANOVA. n = 4 for each condition. C Immunoblot & densitometric analysis of PARP, LC3, & SQSTM1/p62 in HUVECs exposed to N or SS for 1, 2, or 4 h. beta -actin (ACTB) was used as a loading control. P values obtained by unpaired t test (*P 0.01, **P > 0.01); (d) Dynamic uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & starved by HBSS for 3 h. Indicated cells were cultured with 175 KBq 131I for 5, l0, 20, 30, 60, 90 & 120 min. The uptake of 131I in indicated cells was detected by a gamma counter; (e) Radionuclide uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA in the presence or absence of 3-MA (10 mM) treatment for 1 h & then starved by HBSS for 3 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter (n = 3, *P 0.01); (f) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter. Rap, rapamycin. (n = 3, *P 0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416161815.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ROS was sufficient for inducing HMGB1 translocation & enhancing autophagy (a) FTC-133/TPC-1 cells were pretreated with the antioxidant (NAC, 2 mM) for 1 h & then starved by HBSS for 3 h. ROS production was assessed by measuring the fluorescent intensity of DCF on a fluorescent plate reader. Incremental production of ROS was expressed as a percentage of control (n = 3, *P 0.01); (b) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. Flow cytometry was performed for measuring the ROS level by a DCFH-DA probe in indicated cells. Rap, rapamycin. (n = 3, *P 0.01); (c) FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & then starved by HBSS for 3 h. ATP levels were detected by ATP Assay Kit (n = 3, *P > 0.01); (d) FTC-133/TPC-1 cells were pretreated with NAC (2 mM) & then starved by HBSS for 3 h. LC3-I/II, NIS, p-AMPK, AMPK, p-mTOR, mTOR, p-p70S6K & p70S6K levels were assayed by Western blot; (e) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. LC3-I/II, NIS, p-mTOR & mTOR levels were assayed by Western blot. Rap, rapamycin Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416182641.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Fucoxanthin activated autophagy after TBI.(A) Representative images of immunofluorescence for LC3 surrounding the injured cortex. LC3 punctate dots were observed in the cytoplasm by immunofluorescent staining of LC3 (red). Neuron cells & nuclei are labeled with NeuN (green) & DAPI (blue), respectively. Magnification: 40 x. Scale bar: 50 mm. (B) Mice brain tissues were collected 1 day after TBI in different groups, & the expression of LC3, Beclin-1 & p62 was measured by western blot. Fucoxanthin treatment significantly increased the level of LC3-II & Beclin-1 while decreasing the level of p62 after TBI. (C) 3-MA (400 nM) was injected i.c.v. 30 min before TBI. Mice were then subjected to TBI & treatment of fucoxanthin 30 min after TBI. Pretreatment with 3-MA significantly attenuated fucoxanthin-induced activation of autophagy & suppression of apoptosis & oxidative stress in the ipsilateral cortex. Data are presented as mean ± SEM, n = 6 per group; **p 0.01, **P > 0.01); (d) Dynamic uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA & starved by HBSS for 3 h. Indicated cells were cultured with 175 KBq 131I for 5, l0, 20, 30, 60, 90 & 120 min. The uptake of 131I in indicated cells was detected by a gamma counter; (e) Radionuclide uptaking: FTC-133/TPC-1 cells were transfected with HMGB1 shRNA & control shRNA in the presence or absence of 3-MA (10 mM) treatment for 1 h & then starved by HBSS for 3 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter (n = 3, *P 0.01); (f) FTC-133/TPC-1 cells transfected with HMGB1 shRNA & control shRNA were starved by HBSS for 3 h & then treated with rapamycin (1 μM) for 12 h. After 1-h incubating with 131I, the uptake of 131I in indicated cells was detected by a gamma counter. Rap, rapamycin. (n = 3, *P 0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31331356), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616376.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Metformin treatment increases cisplatin effects; (A) MDA-MB-231 & Ca Ski cells were either left untreated or treated with metformin or cisplatin alone or metformin in combination with cisplatin for 15 days. At the end of the treatment, cells were processed to obtain whole cell lysates. MAP1LC3B, pPRKAA2Thr172, PRKAA2 & CASP3 (cleaved) expression was determined by Western blot. ACTB was used as loading control. Densitometric analysis of the gels was performed as described under Materials & Methods; (B) MDA-MB-231 & Ca Ski cells were either left untreated or treated with metformin or cisplatin alone or metformin in combination with cisplatin for 15 days. Ammonia level in the culture medium was measured as indicated in the Material & Methods section. # Significantly different from treatment with metformin alone. All experiments in this figure were repeated three times. * Significantly different from control untreated cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30646605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618938.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Autophagy & the proteasome regulate CagA stability. (A) Wild-type (WT) & autophagy-deficient (Atg5−/−) MEFs were infected with a CagA+ vacA− isogenic mutant strain (MOI 100) for 8 hours using a gentamycin protection assay. The autophagy marker LC3-II was used to confirm that Atg5−/− MEFs are autophagy-deficient. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to WT MEFs (mean + SEM; n = 4). (B) AGS cells were infected with a CagA+ vacA− isogenic mutant strain (MOI 50) for 19 hours using a gentamycin protection assay. MG132 (5 μM) was added during the 14-hour low-dose gentamycin incubation. DMSO was used as a vehicle control. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to vehicle control (mean + SEM; n = 6). (C) AGS cells were infected with a CagA+ vacA− isogenic mutant strain (MOI 50) for 24 hours using a gentamycin protection assay. Lactacystin (10 μM) was added during the 19-hour low-dose gentamycin incubation. Water was used as a vehicle control. CagA protein levels were measured by Western blotting using beta -actin as loading control. Graph shows fold change of CagA normalized to beta -actin relative to vehicle control (mean + SEM; n = 5). Relevant gel bands were cropped from the original blots. Dotted line indicates slicing of two regions together from the same blot. Statistical analysis was performed using Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30631092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416173533.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Vps34 activity is required for maintaining LC3B-ii levels at P10 & mTOR inhibition increases p-Beclin-1 & LC3B-ii levels at P28. (A) Representative Western blot images for actin, DARPP32 & LC3B-i & -ii in striatal slices obtained from P10 or P28 mice, treated with SAR405 (1 μM) or vehicle (Veh; DMSO, 0.1%). (B,C) Quantification of LC3B-ii relative to actin, normalized to vehicle condition at each age. (B) P10: unpaired, two-tailed t-test, t11 = 2.985, p = 0.0124; P28: unpaired, two-tailed t-test, t24 = 1.807, p = 0.0922. P10: Veh: n = 6 slices, SAR405 n = 7 slices from 3 to 4 mice/age. (C) P28: Veh: n = 9 slices, Baf n = 7 slices from 3 to 4 mice/age. *p 0.05 versus untreated group). C. Morphological features of NB4 cells that were treated with ATRA (1 μM) or HMGB1 (1 μg/ml) was determined by Wright-Giemsa staining & visualized by light microscopy (100X magnification). D. Differentiation of NB4 cells treated with ATRA (1 μM) or HMGB1 (10 μg/ml) for 6-48 h was examined by NBT reduction & surface CD11b expression in comparison to the control (DMSO) (n=3, *P<0.05 versus ATRA group). E. Expression of PML-RAR alpha , P62 & LC3-I/II in NB4 cells treated with ATRA (1 μM) or HMGB1 (10 μg/ml) for 48 h was assayed by western blotting & co-immunoprecipitation in comparison to control (DMSO). Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.15432), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416171499.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Zearalenone (ZEN) induced endoplasmic reticulum (ER) stress & autophagy in HepG2 cells. mRNA level & protein expression were determined by quantitative real-time polymerase chain reaction (qRT-PCR) & Western blot analysis, respectively. (A) The protein expression level of GRP78 was measured in cells treated with ZEN for 1 h. (B) The phosphorylation of eIF2 alpha was evaluated in cells treated with ZEN for 2 h. (C) CHOP mRNA levels, (D) Beclin1 mRNA levels, & (E) LC3-II mRNA levels were determined in cells treated with ZEN for 4 h. (F) The protein expression level of LC3-II/LC3-I was examined in cells treated with ZEN for 24 h. Data represent mean ± SEM of three independent experiments. * indicates significant difference vs. the control (** p < 0.01, & *** p < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31861425), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416154612.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ATRA induces autophagy in SKBR3 cells. (a) SKBR3 & MDA-MB-453 breast cancer cells were treated either with 0.1 or 1 μM ATRA for 2 & 4 days, respectively. beta -Catenin & LC3B levels were measured by western blotting. GAPDH was used as a loading control. (b) LC3B-II quantification from at least three independent experiments. LC3B-II expression was normalized to GAPDH & to vehicle-treated SKBR3 cells. (c) beta -Catenin staining of SKBR3 & MDA-MB453 cells. Cells were control or ATRA (1 μM) treated for 2 days. beta -Catenin FITC (fluorescein isothiocyanate) & nuclear DAPI (4',6-diamidino-2-phenylindole) staining as analyzed by confocal microscopy are shown. (d) Quantification of endogenous LC3B puncta. LC3B in SKBR3 & MDA-MB453 cells treated with 1 μM ATRA for 2 days. (e) LC3B-II western blotting & quantification of the autophagic activation upon treatment with 1 μM ATRA for 2 days in the presence or absence of BafA for 2 h at 200 nM. LC3B-II levels were normalized to GAPDH & to vehicle-treated SKBR3 cells. Standard deviations for five independent experiments are shown. (f) Long-lived protein degradation assay of SKBR3 & MDA-MB453 cells treated as in (e). Radioactivity was determined by liquid scintillation counting of at least three independent experiments. Absolute proteolysis is shown. (g) Long-lived protein degradation assay of SKBR3 treated as in (e) & including treatment with the macroautophagy-specific inhibitor 3-MA (10 mM). Analysis as in (f). Mann–Whitney U-test: *P<0.05, **P<0.01, ***P<0.001 & ****P<0.0001 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015236), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616052.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - CA1 Tg mice undergo mitochondrial stress. a WB analysis of extracts from 6-mo Wt & Tg mice CA1 (Wt, n = 6; Tg, n = 7), using antibodies against SIRT3, SOD2 & acetylated SOD2. b WB analysis of extracts from 12-mo Wt & Tg mice hippocampi (Wt, n = 5; Tg, n = 5). Data are presented as mean ± SEM (**P < 0.01; ***P < 0.001). WB analysis of extracts from 6-mo Wt & Tg mice CA1 (Wt, n = 6; Tg, n = 5) (c), & from 12-mo Wt & Tg mice hippocampi (Wt, n = 5; Tg, n = 5) (d) for PINK1 & LC-3. Data are presented as mean ± SEM, *P < 0.05. WB analysis of extracts from 6-mo WT & Tg mice CA1 (WT, n = 5; Tg, n = 6) (e), & from 12-mo WT & Tg mice hippocampi (WT, n = 5; Tg, n = 5) (f) for TFAM. Data are presented as mean ± SEM (*P < 0.05), **P < 0.01). Actin was used as loading control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32131898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241616181.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - ATRA induces autophagy in SKBR3 cells. (a) SKBR3 & MDA-MB-453 breast cancer cells were treated either with 0.1 or 1 μM ATRA for 2 & 4 days, respectively. beta -Catenin & LC3B levels were measured by western blotting. GAPDH was used as a loading control. (b) LC3B-II quantification from at least three independent experiments. LC3B-II expression was normalized to GAPDH & to vehicle-treated SKBR3 cells. (c) beta -Catenin staining of SKBR3 & MDA-MB453 cells. Cells were control or ATRA (1 μM) treated for 2 days. beta -Catenin FITC (fluorescein isothiocyanate) & nuclear DAPI (4',6-diamidino-2-phenylindole) staining as analyzed by confocal microscopy are shown. (d) Quantification of endogenous LC3B puncta. LC3B in SKBR3 & MDA-MB453 cells treated with 1 μM ATRA for 2 days. (e) LC3B-II western blotting & quantification of the autophagic activation upon treatment with 1 μM ATRA for 2 days in the presence or absence of BafA for 2 h at 200 nM. LC3B-II levels were normalized to GAPDH & to vehicle-treated SKBR3 cells. Standard deviations for five independent experiments are shown. (f) Long-lived protein degradation assay of SKBR3 & MDA-MB453 cells treated as in (e). Radioactivity was determined by liquid scintillation counting of at least three independent experiments. Absolute proteolysis is shown. (g) Long-lived protein degradation assay of SKBR3 treated as in (e) & including treatment with the macroautophagy-specific inhibitor 3-MA (10 mM). Analysis as in (f). Mann–Whitney U-test: *P<0.05, **P<0.01, ***P<0.001 & ****P<0.0001 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015236), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-310202416182623.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - Bmi‐1 deficiency aggravates cardiac hypertrophy & decreases autophagic flux. (A) Representative micrographs of paraffin‐embedded heart ventricular wall sections of 6‐week‐old Bmi‐1–/– mice & WT mice stained for haematoxylin‐eosin (H&E), wheat germ agglutinin (WGA) & Masson's trichrome (Masson) staining. (B) Heart weight relative to body weight (HW/BW) & heart weight relative to tibia length (HW/TL). (C) The wall thickness of interventricular septum. (D) Myocyte cross‐sectional area from Bmi‐1–/– mice relative to WT mice. (E) Collagenous fibre area from Bmi‐1–/– mice relative to WT mice was counted with anterior wall staining for Masson. (F) Anp, Bnp, beta ‐MHC, c‐TnI & GATA4 mRNA levels in hearts by real‐time RT‐PCR, calculated as ratio to beta ‐actin mRNA & expressed relative to WT. (G) Western blots of cardiac tissue extracts & mouse embryonic cardiomyocytes (MECs) showing ANP, BNP, GATA4, LC3B & p16; beta ‐actin was the loading control. (H) Protein levels relative to beta ‐actin were assessed by densitometric analysis. (I) Representative micrographs of paraffin‐embedded heart sections immunohistochemical staining for ANP, BNP & GATA4. (J) The percentage of cells positive for ANP, BNP, GATA4 or positive area relative to total cells or area. (K) Representative micrographs of fluorescence with autophagy lentivirus transfection, with DAPI for nuclei. (L) Percentage of positive GFP dots or mRFP dots relative to total cells. (M) The number of autophagosomes & autolysosomes per cell. Six mice per group were used for experiments. Cell experiments were performed with three biological repetitions per group. Values are mean ± SEM from six determinations per group, *p < .05, **p < .01, ***p < .001 compared with WT group, unpaired Student's t‐test Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35390228), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618262.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - 8-Cl-Ado-induces autophagy. Immunoblot analysis of (A) phospho-ULK (Ser555) levels & (B) LC3B-I lipidation to form LC3B-II in MCF-7 & BT-474 cells treated with 10 μM of 8-Cl-Ado for the indicated times. (C) Fluorescent microscopy of MCF-7 & BT-474 cells transiently transfected with GFP-LC3B & treated with 10 μM of 8-Cl-Ado for 12-hours to assess aggregation of LC3B. (D) Immunoblot analysis of p62 levels in MCF-7 & BT-474 cells treated with 10 μM of 8-Cl-Ado for the indicated times. The normalized ratio of p62 to GAPDH relative to the untreated control is indicated beneath each lane. (E) Fluorescent microscopic imaging of autolysosomes. MCF-7 cells were untreated or treated for 2-days with 8-Cl-Ado or rapamycin. Cells were stained with MDC, blue, to visualize AVO & Syto 61 (DNA), red, for nuclei counterstaining. (F) Representative flow cytometery histograms of AVO stained with acridine orange in MCF-7 cells untreated or treated for 3 days with 50 nM rapamycin or 10 μM 8-Cl-Ado. Baf was added before 30 min prior to staining to neutralize AVO staining. (G) Quantification triplicate experiments of MCF-7 & BT-474 cells treated & analyzed as in E. Image collected & cropped by CiteAb from the following publication (//jhoonline.biomedcentral.com/articles/10.1186/1756-8722-7-23), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241617525.jpg)
![Western Blot: LC3B Antibody - BSA Free [NB600-1384] - PB induces autophagy but blocks autophagosome trafficking & autophagosome-lysosome fusion in Hep3B cells.(A) Hep3B cells, HepG2 cells, & primary mouse hepatocytes treated w/ increasing concentrations of PB (6–2000 μg/mL) for 24 h; viable cells quantified using the MTT assay. Data are presented as mean ± SD from at least 3 independent experiments. Bars = SD. *P < 0.05, **P < 0.01, ***P < 0.001, control versus PB-treated cells. (B) Hep3B cells treated for 6, 24 & 48 h w/ indicated concentrations of PB. Levels of protein expression analysed by WB using antibodies against LC3B, p62/SQSTM1, ATG12, BECN1 & Actin. Images cropped from different blots run under the same experimental conditions. The original blots attached as Supplementary Figure 3A. (C) Hep3B cells transfected w/ GFP-LC3B treated w/ 240 μg/mL PB for 24 h & then observed under a confocal microscope. (D) Hep3B cells treated for 24 h w/ indicated concentrations of PB. Levels of protein expression analysed by WB using antibodies against phosphorylated & total mTOR, 4EBP1, & p70S6K1 as well as actin. Images cropped from different blots run under the same experimental conditions. The original blots attached as Supplementary Figure 3B. (E) Hep3B cells serum-starved overnight, & incubated w/ or w/out PB (240 μg/mL) for 6 h before stimulating w/ 20 ng/mL EGF for 20 min. EGFR protein levels analysed by confocal microscope. (F) Hep3B cells treated PB for 12, 24 or 48 h w/ indicated concentrations. Levels of protein expression analysed by WB using antibodies against EGFR & Actin. Images cropped from different blots run under the same experimental conditions in each panel. The original blots attached as Supplementary Figure 3C. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep41437), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1384_rabbit-polyclonal-lc3b-antibody-31020241618948.jpg)
![Immunocytochemistry/Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Caco-2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with YAP1 Antibody (NB110-58358) at 1 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-58358-img0014.jpg "Immunocytochemistry/Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Caco-2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with YAP1 Antibody (NB110-58358) at 1 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.")
![<b>Biological Strategies Validation. </b>Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - LW6 attenuates the accumulation of cellular YAP1 and its nuclear location. After treating PANC-1 cells with LW6 for 12 hours, LW6 decreased the accumulation of YAP1 when compared to Sham treated cells. n =5 per group. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31897243/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1 Antibody - BSA Free-Western Blot-NB110-58358-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - YAP/TAZ signaling is not activated by loss of TRAF3. NT, NF2 KO1, and TRAF3 KO1 cells stained for YAP1 and DAPI. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33185187/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-58358-img0015.jpg)
![Immunohistochemistry-Paraffin: YAP1 Antibody - BSA Free [NB110-58358] - YAP1 was detected in immersion fixed paraffin-embedded sections of human placenta using Rabbit Anti-Human YAP1 polyclonal Antibody (Catalog # NB110-58358) at 1:200 for 1 hour at room temperature followed by incubation with the Anti-Rabbit IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC003). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to nuclear and cytoplasm in trophoblast cells.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-58358-img0010.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Analysis in transfected HEK 293 cell lysate using YAP1 antibody. Observed molecular weight 75 kDa.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Western-Blot-NB110-58358-img0003.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Consequences of ORP5 and ORP8 knockdown on downstream MAPK and PI3K/AKT signaling. Protein from MOH parental, single and double ORP knockdowns as well as cells transfected with empty vector control (pLKO.1) were harvested, and 20 ug was subjected to SDS-PAGE and used for Western blotting. Image collected and cropped by CiteAb from the following publication (//www.life-science-alliance.org/lookup/doi/10.26508/lsa.201900431), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Western-Blot-NB110-58358-img0012.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - YAP1 Antibody [NB110-58358] - Actomyosin activity inhibits beta-catenin- and YAP-driven proliferation of confluent keratinocytes. Effects of cell density and actomyosin activity on YAP phosphorylation. HaCaT cells cultured for 40 h under the sparse and confluent conditions were treated with 100 uM blebbistatin (Blebb) or DMSO (for control) for 6 h, and then lysed and immunoblotted for Ser127-phosphorylated YAP (pYAP), YAP, beta-catenin and actin. Similar results were obtained in two independent experiments. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep46326), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Western-Blot-NB110-58358-img0011.jpg)
![Simple Western: YAP1 Antibody - BSA Free [NB110-58358] - Simple Western lane view shows a specific band for YAP1 in 0.1 mg/ml of HeLa lysate. Observed molecular weight is 75 kDa. This experiment was performed under reducing conditions using the 12-230kDa separation system.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Simple-Western-NB110-58358-img0007.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human YAP1 Polyclonal Antibody (Catalog # NB110-58358) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for YAP1 at approximately 75 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Knockout-Validated-NB110-58358-img0008.jpg)
![<b>Genetic Strategies Validation. </b>Simple Western: YAP1 Antibody - BSA Free [NB110-58358] - Western lane view shows lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. A specific band was detected for YAP1 at approximately 81 kDa (as indicated) using 50 ug/mL of Rabbit Anti-YAP1 Polyclonal Antibody (Catalog # NB110-58358). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/YAP1-Antibody---BSA-Free-Knockout-Validated-NB110-58358-img0009.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Yap deficiency suppresses cell proliferation in vivo & in vitro. (A-F) The Ki67 positive ratio of lens epithelial cells decreased in Yap-deficient mice at different stages (arrowheads indicate Ki67 positive cells). (G) The relative number of Ki67 positive lens epithelial cells (number of Ki67 positive lens epithelial cells / lens epithelium area). The data are shown as mean ± S.E.M. (Student’s t-test, *P<0.05, **P<0.01, n=10). (H-I) Knockdown efficiency of Yap in alpha TN4 cell using siRNA. (J-K) Cell viability & growth assay revealed that proliferation was downregulated in Yap knockdown alpha TN4 cells. The data are shown as mean ± S.E.M. (Two-way RM ANOVA, **P<0.01, n=5). Scale bars: 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-31020241535689.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Synergistic effect of LW6 & metformin on YAP1. 80 µM LW6, 20 mM metformin (Met) & the combinational treatment metformin plus LW6 increased phosphorylation of YPA1 at serine 127 & decreased cellular YAP1 concentration after treating cells for 24 hours (A). Moreover, this combinational therapy attenuated the nuclear localization of YAP1 compared to Sham treated cells (B). In addition, lysophosphatidic acid (LPA) & the phosphorylation deficient mutant YAP1-S127A stimulate cell migration of 6606PDA cells (C & D). n = 2 per group for A, n = 3 per group for B, n = 7 per group for C, n = 9 per group for D. Bar = 5µm. Arrows point to nuclei. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31897243), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202415371934.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Consequences of ORP5 & ORP8 knockdown on downstream MAPK & PI3K/AKT signaling.Protein from BxPC-3, PANC-1, MiaPaCa-2, & MOH parental, single & double ORP knockdowns as well as cells transfected with empty vector control (pLKO.1) were harvested, & 20 μg was subjected to SDS–PAGE & used for Western blotting. EGFR, MAPK, & PI3K signaling were assayed as pEGFR, ppERK, & pAKT levels, respectively. Amplification of YAP-1 was also evaluated. Total ERK, total AKT, & beta -actin levels were used as loading controls. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31451509), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202415291931.jpg)
![Western Blot: YAP1 Antibody - BSA Free [NB110-58358] - Ajuba depletion induces beta -catenin translocation & Cyclin D1 expression in HCC cell lines. a Immunoblotting with specific antibodies against Ajuba, E-cadherin, beta -catenin, Cyclin D1, YAP, TAZ & CYR61 in Ajuba-depleted BEL7402 & HepG2 cells. GAPDH was used as a loading control. The ratios of expression E-Cadherin to their corresponding GAPDH are represented. b Ajuba-depleted HCC cells were fixed for immunofluorescence & stained for beta -catenin protein (green) & DAPI (blue). Representative merged images are also shown for fluorescence signals. Scale bar = 25 μm. c Correlation of Ajuba expression with OS in HCC. Low expression of Ajuba was associated with worse OS compared to high expression of Ajuba. Kaplan-Meier curves & log-rank test were used to evaluate OS. P < 0.05 was considered significant. d, e Representative images & quantification of migration & invasion of Ajuba-depleted (d) or Ajuba-overexpressing (e) HCC cells. Scale bar = 200 μm. HCC, hepatocellular carcinoma. f Expression in response to the overexpression of constructs of Ajuba-Myc was examined by IB, the ratios of expression Ajuba to their corresponding GAPDH are represented. Data are presented as Mean ± SEM from three independent experiments (*p < 0.05, **p < 0.01, ***p < 0.001) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30041665), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235517.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - YAP & TAZ expression at high density & during chondrogenic differentiation of human synovial MSCs. (A) YAP & pYAP expression in human synovial membrane-derived (hSM-)MSCs in monolayer at low (L) & high (H) density detected by immunofluorescence staining, shown without (i) & with sytox green nuclear counterstain (ii). (B) YAP & pYAP expression in hSM-MSCs in monolayer at low (L) & high (H) density detected by western blotting with beta -actin as loading control. (C, D) Expression of YAP & TAZ (C) & their target genes CTGF & CYR61 (D) in hSM-MSCs immediately prior to (0 h) or 24 h after plating in micromass culture, determined by quantitative RT-PCR. Data was normalised to GAPDH expression, & is shown as mean ± standard deviation (SD) (three donors) relative to pre-seeding (0 h) control. *P <0.05; **P <0.01; ***P <0.001. (E) Expression of YAP & TAZ in hSM-MSCs after 6 days of treatment with 10 ng/ml TGF-beta 1 or vehicle only in micromass culture to induce chondrogenic differentiation, determined by quantitative RT-PCR. Data was normalised to GAPDH expression, & is shown as mean ± SD (five donors) relative to vehicle-treated control. *P <0.05. (F) Detection of YAP by western blotting during chondrogenic differentiation induced by TGF-beta 1 with detection of beta -actin as loading control. MSC, mesenchymal stromal/stem cell; pYAP, phosphorylated YAP; RT-PCR, reverse transcription PCR; TAZ, transcriptional co-activator with PDZ-binding motif; TGF, transforming growth factor; YAP, Yes-associated protein. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26025096), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235539.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Expression of spcCre is associated with loss of YAP in SOX9+ distal airways.(A–D) Immunostaining of lung sections collected from Yapf/f; spcCre/+ mice at 13.5 days post coitus (dpc). SOX2 expression marks the proximal airway, while the distal airway is distinguished by SOX9 expression (not shown). High levels of spcCre expression were largely confined to the distal airway, where spcCre expression in a given epithelial cell was correlated with loss of YAP immunoreactivity (e.g. arrowheads in D). (E–H) Immunostaining of lung sections collected from Yapf/f; spcCre/+ mice at 14.5 dpc. Only distal airways are shown. YAP was lost mainly in distal airways in Yapf/f; spcCre/+ mice while sporadic loss of YAP was found in the proximal airway. Loss of YAP was most apparent in the more distal part (arrow in H) of the distal airway, while residual YAP could be found in the more proximal part of the distal airway. Together, these results suggest that lung cyst formation in distal airways of Yapf/f; spcCre/+ mice is due to loss of YAP in the distal airway. Scale bar = 25 μm for A–D; E–H.DOI://dx.doi.org/10.7554/eLife.21130.012 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235526.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - The expression patterns of Yap & GFAP-Cre recombinase in postnatal mouse eyes. (A) Schematic of a transverse section of mouse eye. (B-C) Immunostaining with anti-Yap antibody (green) on frozen eye sections at different ages. Nuclei were counterstained with DAPI (blue). Yap staining was detected in scattered cells within the INL (arrowheads) & GCL of the retina & the lens epithelium (arrows). (D) Cre recombinase (red) was expressed in the lens epithelium & INL, GCL of retina in frozen eye sections of Tomatof/+; GFAP-Cre mice at P14. Nuclei were counterstained with DAPI (blue). LE, lens epithelium; TZ, transitional zone; RPE, retinal pigment epithelium; OS, outer segment; IS, inner segment; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer. Scale bars: 25 μm (B-C), 100 μm (D). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235548.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - YAP & phospho-YAP are detected in both the proximal & distal airways during lung development.(A–H) Immunostaining of lung sections collected from wild-type mice at 13.5 days post coitus (dpc). The proximal airway is marked by SOX2 expression, while the distal airway is distinguished by SOX9 expression (not shown). Nuclear YAP can be frequently found in both SOX2+ & SOX9+ domains. Similarly, phospho-YAP at S112 (pYAP) could be detected in both the proximal & distal airways. pYAP levels were, in general, higher in the proximal than distal epithelium but pYAP levels varied significantly from cell to cell in both the proximal & distal airways. Representative cells with higher levels of pYAP (arrowhead) are indicated in (B,F). In many cells, low levels of pYAP were associated with the presence of nuclear YAP. This is consistent with a model in which pYAP is sequestered by 14-3-3 proteins in the cytoplasm & degraded but also indicate a dynamic shuttling & distribution of YAP along the entire airway epithelium. Similar results were obtained for lungs collected at 12.5 dpc. Scale bar = 7.5 μm for A–H.DOI://dx.doi.org/10.7554/eLife.21130.005 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-31020241623554.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Expression of Nkx2.1Cre is associated with loss of YAP in the upper lobes.(A–D) Immunostaining of lung sections collected from Yapf/f; Nkx2.1Cre/+ mice at 14.5 days post coitus (dpc). SOX2 expression marks the proximal airway, while the distal airway is distinguished by SOX9 expression (not shown). YAP was lost mainly in the upper lobe in Yapf/f; Nkx2.1Cre/+ lung. Loss of YAP was more apparent in the distal airway, while loss of YAP was sporadic in the proximal airway. Lung cyst formation was primarily observed in the distal airway. The boxed region in (B) indicates areas shown in (C,D). Scale bar = 250 μm for A,B; 250 μm for C,D. Sox2 expression was present in sporadic Yap-deficient cells in the transition zone induced by Sox9Cre, spcCre or Nkx2.1Cre. This suggests that Sox2 expression is not controlled by YAP.DOI://dx.doi.org/10.7554/eLife.21130.013 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235520.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - Active nuclear YAP is distributed throughout the mouse lung epithelium during development.(A–P) Immunostaining of lung sections collected from wild-type mice at 11.5 & 12.5 days post coitus (dpc). The boxed region in (L) indicates areas shown in (N–P). The proximal airway is marked by SOX2 expression, while the distal airway is distinguished by SOX9 expression. Nuclear YAP can be frequently found in both SOX2+ & SOX9+ domains & is not restricted to the junction (the ‘transition zone’) between SOX2+ & SOX9+ domains. Representative cells with nuclear YAP (arrowhead) are indicated in (E,P). YAP immunoreactivity is completely absent in the epithelium (but present in the mesenchyme) of Yapf/f; ShhCre/+ mice (M), demonstrating the specificity of YAP antibodies used in this study. Immunofluorescence & immunohistochemistry yielded the same results (data not shown for immunohistochemistry). (Q–R) Whole-mount immunostaining of wild-type & Yap mutant lungs at 11.5 dpc. Distinct domains of SOX2 were discerned in the absence of YAP. Scale bar = 10 μm for A–J; 25 μm for K, L; 10 μm for N–P; 50 μm for Q, R.DOI://dx.doi.org/10.7554/eLife.21130.004 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28323616), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-310202416235530.jpg)
![Immunocytochemistry/ Immunofluorescence: YAP1 Antibody - BSA Free [NB110-58358] - The expression patterns of Yap & GFAP-Cre recombinase in postnatal mouse eyes. (A) Schematic of a transverse section of mouse eye. (B-C) Immunostaining with anti-Yap antibody (green) on frozen eye sections at different ages. Nuclei were counterstained with DAPI (blue). Yap staining was detected in scattered cells within the INL (arrowheads) & GCL of the retina & the lens epithelium (arrows). (D) Cre recombinase (red) was expressed in the lens epithelium & INL, GCL of retina in frozen eye sections of Tomatof/+; GFAP-Cre mice at P14. Nuclei were counterstained with DAPI (blue). LE, lens epithelium; TZ, transitional zone; RPE, retinal pigment epithelium; OS, outer segment; IS, inner segment; ONL, outer nuclear layer; OPL, outer plexiform layer; INL, inner nuclear layer; IPL, inner plexiform layer; GCL, ganglion cell layer. Scale bars: 25 μm (B-C), 100 μm (D). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31011480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-58358_rabbit-polyclonal-yap1-antibody-31020241623552.jpg)
![Western Blot: YAP1 Antibody (1A12) [NBP2-22117] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:500 of Mouse Anti-Human YAP1 Monoclonal Antibody (Catalog # NBP2-22117) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific band was detected for YAP1 at approximately 75 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-Knockout-Validated-NBP2-22117-img0010.jpg "<b>Genetic Strategies Validation. </b>Western Blot: YAP1 Antibody (1A12) [NBP2-22117] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:500 of Mouse Anti-Human YAP1 Monoclonal Antibody (Catalog # NBP2-22117) followed by HRP-conjugated Anti-Mouse IgG Secondary Antibody (Catalog # HAF018). Specific band was detected for YAP1 at approximately 75 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.")
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: YAP1 Antibody (1A12) - BSA Free [NBP2-22117] - Caco-2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with YAP1 Antibody [1A12] (NBP2-22117) at 1 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-BSA-Free-Immunocytochemistry-Immunofluorescence-NBP2-22117-img0012.jpg)
![Immunohistochemistry-Paraffin: YAP1 Antibody (1A12) [NBP2-22117] - Analysis of paraffin-embedded prostate cancer tissues using YAP1 mouse mAb with DAB staining. 1:200 - 1:1000](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-Immunohistochemistry-Paraffin-NBP2-22117-img0009.jpg)
![Western Blot: YAP1 Antibody (1A12) [NBP2-22117] - Analysis using YAP1 mouse mAb against Hela (1), C6 (2) and Cos7 (3) cell lysate. Dilution 1:500 - 1:2000.](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-Western-Blot-NBP2-22117-img0008.jpg)
![Immunohistochemistry-Paraffin: YAP1 Antibody (1A12) [NBP2-22117] - Analysis of paraffin-embedded rectum cancer tissues using YAP1 mouse mAb with DAB staining. 1:200 - 1:1000](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-Immunohistochemistry-Paraffin-NBP2-22117-img0006.jpg)
![Flow Cytometry: YAP1 Antibody (1A12) [NBP2-22117] - Analysis of Hela cells using YAP1 mouse mAb (green) and negative control (red). Dilution 1:200 - 1:400.](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-Flow-Cytometry-NBP2-22117-img0004.jpg)
![ELISA: YAP1 Antibody (1A12) [NBP2-22117] - Red: Control Antigen (100 ng); Purple: Antigen (10 ng); Green: Antigen (50 ng); Blue: Antigen (100 ng). Dilution 1:10000.](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-ELISA-NBP2-22117-img0001.jpg)
![<b>Genetic Strategies Validation. </b>Simple Western: YAP1 Antibody (1A12) [NBP2-22117] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and YAP1 knockout (KO) HeLa cell line. A specific band was detected for YAP1 at approximately 81 kDa (as indicated) using 20 ug/mL of mouse Anti-YAP1 Monoclonal Antibody (Catalog # NBP2-22117). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/YAP1-Antibody-1A12-Knockout-Validated-NBP2-22117-img0011.jpg)
![SDS-Page: Recombinant Human YAP1 Protein [H00010413-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.](http://images.novusbio.com/fullsize/Recombinant-Human-YAP1-Protein-SDS-Page-H00010413-P01-img0002.jpg "SDS-Page: Recombinant Human YAP1 Protein [H00010413-P01] - 12.5% SDS-PAGE Stained with Coomassie Blue.")